Copper in PDB 7xmd: Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4

Enzymatic activity of Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4

All present enzymatic activity of Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4:
7.1.1.3;

Other elements in 7xmd:

The structure of Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4 also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4 (pdb code 7xmd). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4, PDB code: 7xmd:

Copper binding site 1 out of 1 in 7xmd

Go back to Copper Binding Sites List in 7xmd
Copper binding site 1 out of 1 in the Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cryo-Em Structure of Cytochrome BO3 From Escherichia Coli, the Structure Complexed with An Allosteric Inhibitor N4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu703

b:86.4
occ:1.00
 NE2 A:HIS334 2.0 66.9 1.0
NE2 A:HIS333 2.0 67.6 1.0
ND1 A:HIS284 2.0 66.6 1.0
CE1 A:HIS334 2.3 66.9 1.0
CE1 A:HIS333 2.6 67.6 1.0
CE1 A:HIS284 2.8 66.6 1.0
CG A:HIS284 3.1 66.6 1.0
CD2 A:HIS333 3.2 67.6 1.0
CD2 A:HIS334 3.3 66.9 1.0
ND1 A:HIS334 3.5 66.9 1.0
CB A:HIS284 3.6 66.6 1.0
NA A:HEO701 3.8 69.8 1.0
ND1 A:HIS333 3.9 67.6 1.0
C1A A:HEO701 4.0 69.8 1.0
CG A:HIS334 4.0 66.9 1.0
NE2 A:HIS284 4.0 66.6 1.0
FE A:HEO701 4.0 69.8 1.0
CD2 A:HIS284 4.2 66.6 1.0
CG A:HIS333 4.2 67.6 1.0
CHA A:HEO701 4.2 69.8 1.0
ND A:HEO701 4.2 69.8 1.0
C4A A:HEO701 4.3 69.8 1.0
C4D A:HEO701 4.3 69.8 1.0
CA A:HIS284 4.3 66.6 1.0
CG1 A:VAL287 4.6 66.2 1.0
NB A:HEO701 4.6 69.8 1.0
C2A A:HEO701 4.6 69.8 1.0
C3A A:HEO701 4.8 69.8 1.0
CHB A:HEO701 4.8 69.8 1.0
C1B A:HEO701 4.9 69.8 1.0

Reference:

Y.Nishida, S.Yanagisawa, R.Morita, H.Shigematsu, K.Shinzawa-Itoh, H.Yuki, S.Ogasawara, K.Shimuta, T.Iwamoto, C.Nakabayashi, W.Matsumura, H.Kato, C.Gopalasingam, T.Nagao, T.Qaqorh, Y.Takahashi, S.Yamazaki, K.Kamiya, R.Harada, N.Mizuno, H.Takahashi, Y.Akeda, M.Ohnishi, Y.Ishii, T.Kumasaka, T.Murata, K.Muramoto, T.Tosha, Y.Shiro, T.Honma, Y.Shigeta, M.Kubo, S.Takashima, Y.Shintani. Identifying Antibiotics Based on Structural Differences in the Conserved Allostery From Mitochondrial Heme-Copper Oxidases. Nat Commun V. 13 7591 2022.
ISSN: ESSN 2041-1723
PubMed: 36481732
DOI: 10.1038/S41467-022-34771-Y
Page generated: Tue Apr 4 23:31:39 2023

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